Conformational effect of phosphorylation on T cell receptor/CD3 zeta-chain sequences.
The effect of tyrosine-phosphorylation on the conformation of three tyrosine-based immunoreceptor activation motifs, zeta(69-86), zeta(106-126), and zeta(138-155), located in the T cell receptor/CD3 zeta-chain was investigated. Circular dichroism and Fourier-transform infrared spectroscopy of the nonphosphorylated and phosphorylated fragments gave evidence that phosphorylation can alter the secondary structure of the peptides. The most significant--alpha-helix to beta-sheet--conformational change was observed in the case of the zeta(138-155) peptide sequence which may be relevant to recognition by Src homology 2 (SH2) domains of signaling proteins.
Laczkó
I
I
Institute of Biophysics, Biological Research Center, Szeged, Hungary. laczko@everx.szbk.u-szeged.hu
Hollósi
M
M
Vass
E
E
Hegedüs
Z
Z
Monostori
E
E
Tóth
G K
GK
D000595:Amino Acid Sequence; D017252:CD3 Complex / Q000737:chemistry*; D002942:Circular Dichroism; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011948:Receptors, Antigen, T-Cell / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D018909:src Homology Domains / Q000502:physiology
D017252:CD3 Complex; D010446:Peptide Fragments; D011948:Receptors, Antigen, T-Cell; D019000:Phosphotyrosine